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Literature summary for 2.1.2.1 extracted from

  • Anderson, D.D.; Woeller, C.F.; Chiang, E.P.; Shane, B.; Stover, P.J.
    Serine hydroxymethyltransferase anchors de novo thymidylate synthesis pathway to nuclear lamina for DNA synthesis (2012), J. Biol. Chem., 287, 7051-7062.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information recombinant dominant negative SHMT1, DN2-SHMT1, localizes with lamin B1 and enhances SHMT1 activity for de novo thymidylate biosynthesis Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression of a dominant negative, tetracycline-inducible SHMT1 protein, DN2-SHMT1, in HeLa and SH-SY5Y cells, expression of RFP-tagged SHMT2alpha and of YFP- or FLAG-tagged SHMT1 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm SHMT1 encodes the cytoplasmic/nuclear isozyme SHMT1, SHMT2 encodes the mitochondrial isozyme SHMT2 and the cytoplasmic/nuclear isozyme SHMT2alpha through alternative promoter uses Homo sapiens 5737
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mitochondrion SHMT2 encodes the mitochondrial isozyme SHMT2 and the cytoplasmic/nuclear isozyme SHMT2alpha through alternative promoter uses Homo sapiens 5739
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nucleus SHMT1 encodes the cytoplasmic/nuclear isozyme SHMT1, SHMT2 encodes the mitochondrial isozyme SHMT2 and the cytoplasmic/nuclear isozyme SHMT2alpha through alternative promoter uses. SHMT1, SHMT2alpha, thymidylate synthase, and dihydrofolate reductase are present in nuclei during S and G2/M phases Homo sapiens 5634
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzymes by tandem affinity purification, immunoprecipitation, heat treatment, Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
additional information SHMT2alpha co-localizes with lamin B1 in SH-SY5Y cells. Recombinant dominant negative SHMT1, DN2-SHMT1, localizes with lamin B1 and enhances SHMT1 activity for de novo thymidylate biosynthesis Homo sapiens
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Synonyms

Synonyms Comment Organism
serine hydroxymethyltransferase
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Homo sapiens
serine hydroxymethyltransferase 1
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Homo sapiens
serine hydroxymethyltransferase 2alpha
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Homo sapiens
SHMT
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Homo sapiens
SHMT1
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Homo sapiens
SHMT2alpha
-
Homo sapiens

General Information

General Information Comment Organism
metabolism the de novo thymidylate biosynthetic pathway forms a multienzyme complex, containing enzymes serine hydroxymethyltransferase 1 and 2alpha, thymidylate synthase, and dihydrofolate reductase, the complex is associated with the nuclear lamina, overview. The de novo thymidylate biosynthetic pathway in mammalian cells translocates to the nucleus for DNA replication and repair. SHMT1 or SHMT2alpha are required for co-localization of dihydrofolate reductase, SHMT, and thymidylate synthase to the nuclear lamina, indicating that SHMT serves as scaffold protein that is essential for complex formation, SHMT1 scaffold function can determine de novo thymidylate synthesis capacity, SHMT1 interaction with TYMS and DHFR is DNA-dependent, but the formation of thymidylate biosynthesis complex is nucleotide-independent. Folate-mediated one-carbon metabolism in the cytoplasm and nucleus, overview Homo sapiens
physiological function functional redundancy of SHMT2alpha and SHMT1 in nuclear de novo thymidylate synthesis. The de novo thymidylate biosynthetic pathway forms a multienzyme complex, containing enzymes serine hydroxymethyltransferase 1 and 2alpha, thymidylate synthase, and dihydrofolate reductase, the complex is associated with the nuclear lamina, overview. The de novo thymidylate biosynthetic pathway in mammalian cells translocates to the nucleus for DNA replication and repair. SHMT1 or SHMT2alpha are required for co-localization of dihydrofolate reductase, SHMT, and thymidylate synthase to the nuclear lamina, indicating that SHMT serves as scaffold protein that is essential for complex formation. SHMT expression is rate-limiting for de novo thymidylate synthesis Homo sapiens